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AB198766

Recombinant human PARP2 protein

Recombinant human PARP2 protein

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(1 Publication)

Recombinant human PARP2 protein is a Human Full Length protein, in the 2 to 583 aa range, expressed in Baculovirus infected Sf9 cells, with >12%, suitable for SDS-PAGE, FuncS.

別名を表示する

ADPRT2, ADPRTL2, PARP2, Poly [ADP-ribose] polymerase 2, PARP-2, hPARP-2, ADP-ribosyltransferase diphtheria toxin-like 2, DNA ADP-ribosyltransferase PARP2, NAD(+) ADP-ribosyltransferase 2, Poly[ADP-ribose] synthase 2, Protein poly-ADP-ribosyltransferase PARP2, ARTD2, ADPRT-2, pADPRT-2

2 Images
Functional Studies - Recombinant human PARP2 protein (AB198766)
  • FuncS

Supplier Data

Functional Studies - Recombinant human PARP2 protein (AB198766)

Activity assay using ab198766.

SDS-PAGE - Recombinant human PARP2 protein (AB198766)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant human PARP2 protein (AB198766)

10% SDS-PAGE analysis of 2 μg ab198766 with Coomassie staining.

Key facts

精製度

>12% SDS-PAGE

発現系

Baculovirus infected Sf9 cells

タグ

GST tag N-Terminus

アプリケーション

SDS-PAGE, FuncS

applications

生物活性

Yes

生物学的活性

Unit Definition: One unit of PARP incorporates 100 pmoles of poly(ADP) in 1 minute from NAD into the acid-insoluble form.

Assay Conditions: Enzyme reaction is conducted using a PARP2 Assay Kit at room temperature for 1 hour.

アクセッション番号

Q9UGN5

アニマルフリー

No

キャリアフリー

No

種

Human

バッファー組成

pH: 8 Constituents: 20% Glycerol (glycerin, glycerine), 0.64% Sodium chloride, 0.63% Tris HCl, 0.49% Glutathione, 0.05% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.02% Potassium chloride

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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配列情報

[{"sequence":"AARRRRSTGGGRARALNESKRVNNGNTAPEDSSPAKKTRRCQRQESKKMPVAGGKANKDRTEDKQDGMPGRSWASKRVSESVKALLLKGKAPVDPECTAKVGKAHVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTKNNWEDREKFEKVPGKYDMLQMDYATNTQDEEETKKEESLKSPLKPESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHGRALMEACNEFYTRIPHDFGLRTPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQHYRNLHCALRPLDHESYEFKVISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEKEAFREDLHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSEVALGQCNELLEANPKAEGLLQGKHSTKGLGKMAPSSAHFVTLNGSTVPLGPASDTGILNPDGYTLNYNEYIVYNPNQVRMRYLLKVQFNFLQLW","proteinLength":"Full Length","predictedMolecularWeight":"92 kDa","actualMolecularWeight":null,"aminoAcidEnd":583,"aminoAcidStart":2,"nature":"Recombinant","expressionSystem":"Baculovirus infected Sf9 cells","accessionNumber":"Q9UGN5","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]
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出荷温度及び保存条件

出荷温度
Dry Ice
短期保存温度
-80°C
長期保存温度
-80°C
保管に関する情報
Avoid freeze / thaw cycle
True
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補足情報

This supplementary information is collated from multiple sources and compiled automatically.

PARP2 also known as Poly (ADP-ribose) polymerase 2 plays an important role in the repair of damaged DNA. This protein has a molecular mass of approximately 62 kDa. Researchers usually find PARP2 expression in the nucleus primarily in cells undergoing stress or damage responses. The PARP2 protein interacts with substrates during the DNA repair process facilitating the attachment of ADP-ribose polymers to target proteins which is a critical step in the cellular response to DNA strand breaks.
Biological function summary

Poly (ADP-ribose) polymerase 2 serves a critical function in maintaining genomic stability. This protein is part of the PARP protein family and operates in conjunction with PARP1. Together they form a complex that senses DNA damage and initiates the repair mechanism. This action helps prevent mutations and genome rearrangements which could otherwise lead to cell death or oncogenesis.

Pathways

PARP2 contributes significantly to the base excision repair (BER) and homologous recombination (HR) pathways. It collaborates with other repair enzymes and kinases like XRCC1 and DNA-PKcs to effectively mediate the repair processes. The activity of PARP2 ensures prompt and accurate repair of single-strand and double-strand DNA breaks allowing these pathways to maintain cellular homeostasis and integrity.

PARP2 associates prominently with cancer and neurodegenerative diseases. Due to its DNA repair function improper regulation or expression of PARP2 may lead to an increased risk of tumorigenesis making it a target for cancer therapy. Additionally disorders like Alzheimer's disease show an association with PARP2 due to its relationship with oxidative stress and DNA damage. Therapies targeting PARP2 along with PARP1 represent a promising approach in treating these conditions by enhancing DNA repair or inducing synthetic lethality in cancer cells.
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製品の性状

製品の状態

Liquid

補足情報

Affinity purified.

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一般的な情報

機能

Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair (PubMed : 10364231, PubMed : 25043379, PubMed : 27471034, PubMed : 30104678, PubMed : 32028527, PubMed : 32939087, PubMed : 34108479, PubMed : 34486521, PubMed : 34874266). Mediates glutamate, aspartate or serine ADP-ribosylation of proteins : the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units (PubMed : 25043379, PubMed : 30104678, PubMed : 30321391). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed : 32939087). Mediates glutamate and aspartate ADP-ribosylation of target proteins in absence of HPF1 (PubMed : 25043379). Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 conferring serine specificity by completing the PARP2 active site (PubMed : 28190768, PubMed : 32028527, PubMed : 34108479, PubMed : 34486521, PubMed : 34874266). PARP2 initiates the repair of double-strand DNA breaks : recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones, thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks (PubMed : 10364231, PubMed : 32939087, PubMed : 34108479). HPF1 initiates serine ADP-ribosylation but restricts the polymerase activity of PARP2 in order to limit the length of poly-ADP-ribose chains (PubMed : 34732825, PubMed : 34795260). Specifically mediates formation of branched poly-ADP-ribosylation (PubMed : 30104678). Branched poly-ADP-ribose chains are specifically recognized by some factors, such as APLF (PubMed : 30104678). In addition to proteins, also able to ADP-ribosylate DNA : preferentially acts on 5'-terminal phosphates at DNA strand breaks termini in nicked duplex (PubMed : 27471034, PubMed : 29361132).

配列の類似性

Belongs to the ARTD/PARP family.

翻訳後修飾

Auto poly-ADP-ribosylated on serine residues, leading to dissociation of the PARP2-HPF1 complex from chromatin (PubMed:32939087, PubMed:34108479). Poly-ADP-ribosylated by PARP1 (By similarity).. Acetylation reduces DNA binding and enzymatic activity.. Proteolytically cleaved by caspase-8 (CASP8) in response to apoptosis, leading to its inactivation.

細胞内局在性

Nucleus

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製品プロトコール

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ターゲットの情報

Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair (PubMed : 10364231, PubMed : 25043379, PubMed : 27471034, PubMed : 30104678, PubMed : 32028527, PubMed : 32939087, PubMed : 34108479, PubMed : 34486521, PubMed : 34874266). Mediates glutamate, aspartate or serine ADP-ribosylation of proteins : the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units (PubMed : 25043379, PubMed : 30104678, PubMed : 30321391). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed : 32939087). Mediates glutamate and aspartate ADP-ribosylation of target proteins in absence of HPF1 (PubMed : 25043379). Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 conferring serine specificity by completing the PARP2 active site (PubMed : 28190768, PubMed : 32028527, PubMed : 34108479, PubMed : 34486521, PubMed : 34874266). PARP2 initiates the repair of double-strand DNA breaks : recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones, thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks (PubMed : 10364231, PubMed : 32939087, PubMed : 34108479). HPF1 initiates serine ADP-ribosylation but restricts the polymerase activity of PARP2 in order to limit the length of poly-ADP-ribose chains (PubMed : 34732825, PubMed : 34795260). Specifically mediates formation of branched poly-ADP-ribosylation (PubMed : 30104678). Branched poly-ADP-ribose chains are specifically recognized by some factors, such as APLF (PubMed : 30104678). In addition to proteins, also able to ADP-ribosylate DNA : preferentially acts on 5'-terminal phosphates at DNA strand breaks termini in nicked duplex (PubMed : 27471034, PubMed : 29361132).
See full target information PARP2
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文献 (1)

Recent publications for all applications. Explore the full list and refine your search

Cell reports 27:3124-3138.e13 PubMed31189100

2019

Poly(ADP-Ribose) Links the DNA Damage Response and Biomineralization.

Applications

Unspecified application

Species

Unspecified reactive species

Karin H Müller,Robert Hayward,Rakesh Rajan,Meredith Whitehead,Andrew M Cobb,Sadia Ahmad,Mengxi Sun,Ieva Goldberga,Rui Li,Uliana Bashtanova,Anna M Puszkarska,David G Reid,Roger A Brooks,Jeremy N Skepper,Jayanta Bordoloi,Wing Ying Chow,Hartmut Oschkinat,Alex Groombridge,Oren A Scherman,James A Harrison,Anja Verhulst,Patrick C D'Haese,Ellen Neven,Lisa-Maria Needham,Steven F Lee,Catherine M Shanahan,Melinda J Duer
View all publications
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